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Full-Text Articles in Life Sciences
Mutating Tetur02g09850 Originated From Spider Mites To Enhance Crystallization, Hayley Cash
Mutating Tetur02g09850 Originated From Spider Mites To Enhance Crystallization, Hayley Cash
Senior Theses
This study aimed to explain and adequately utilize several common biochemical laboratory techniques to mutate a portion of the nucleic acid sequence within a specific protein. This protein, referred to as Tetur02g09850 is originated from Tetranychus Urticae, or the Two-Spotted Spider Mite. This mite causes excessive damage to crops and is known to be extremely resistant to most common pesticides. For this reason, understanding the protein structure could be used to explain this acaricide resistance and aid in the development of more effective pesticides. Some of the testing utilized was site-directed mutagenesis, IMAC and gel filtration for protein purification, gel …
Functional Characterization Of Cancer-Related Mutations Of Erk3, Hadel Mohammed Alsaran
Functional Characterization Of Cancer-Related Mutations Of Erk3, Hadel Mohammed Alsaran
Browse all Theses and Dissertations
Extracellular signal-regulated kinase 3 (ERK3) is an atypical member of the mitogen-activated protein kinase (MAPK) family. Recent studies have shown that ERK3 is highly upregulated in multiple cancers, such as lung cancer and colon cancer. Importantly, ERK3 promotes cancer cell migration and invasion by phosphorylating steroid receptor activator 3 (SRC-3), hence upregulating pro-invasive matrix metalloproteinase genes. While the link between ERK3 and cancers has been recognized, little is known about ERK3 mutations in cancer progression. In this study, we have investigated ERK3 mutations on arginine 64 (arginine 64 mutated to cysteine or histidine, R64C or R64H) and leucine 290 (leucine …
Subunit Interactions Of Recombinant Hiv-1 Reverse Transcriptase With Mutations At L289, Jacquelyn R. Smith
Subunit Interactions Of Recombinant Hiv-1 Reverse Transcriptase With Mutations At L289, Jacquelyn R. Smith
Theses and Dissertations in Biomedical Sciences
Reverse transcriptase (RT) is a dimeric enzyme required for replication of the human immunodeficiency virus (HIV). If the subunits of the RT dimer are dissociated, the enzyme is no longer active; therefore, identification of subunit binding sites could lead to potential targets for antiviral therapy. In order to identify where subunit binding of RT occurs, mutations were made at leucine (L) 289, a residue believed to be involved in dimerization through hydrophobic interactions with other leucines. L289 is the central leucine of a leucine repeat sequence which resembles a leucine zipper protein-DNA binding motif. Two mutations, leucine to arginine (L289R) …